A receptor scaffold mediates stimulus-response coupling in bacterial chemotaxis.

The mechanism of stimulus-response coupling in bacterial chemotaxis has emerged as a paradigm for understanding general features of intracellular signal transduction both in bacterial and eukaryotic cells. Until recently it was thought that the mechanism involved reversible stochastic interactions between dimeric receptors freely diffusing in the cytoplasmic membrane and several soluble signal transduction proteins within the cytoplasm. Recent results have shown that this view is an oversimplification. The receptors and most of the signal transduction proteins are organized together in a higher ordered structure at one pole of the bacterial cell. The scaffolding network within this structure appears to be composed of C-terminal alpha-helical extensions of the membrane chemoreceptor proteins held together in a lattice by tandem SH3-like domains. Results suggest that stimuli are detected through the perturbations they induce in scaffolding architecture.